|Other Names||Calpain-10, 3422-, Calcium-activated neutral proteinase 10, CANP 10, CAPN10, KIAA1845|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. May play a role in insulin-stimulated glucose uptake.|
|Tissue Location||Detected in primary skeletal muscle cells (at protein level). Ubiquitous.|
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Provided below are standard protocols that you may find useful for product applications.
CAPN10 is ubiquitous, well-conserved family of calcium-dependent, cysteine proteases. This protein is heterodimers consisting of an invariant small subunit and variable large subunits. The large catalytic subunit has four domains: domain I, the N-terminal regulatory domain that is processed upon calpain activation; domain II, the protease domain; domain III, a linker domain of unknown function; and domain IV, the calmodulin-like calcium-binding domain. It is an atypical calpain in that it lacks the calmodulin-like calcium-binding domain and instead has a divergent C-terminal domain. The protein is similar in organization to calpains 5 and 6.
Unsal,T., Konac,E. J. Assist. Reprod. Genet. 26 (4), 205-216 (2009)Garcia-Escalante,M.G. Invest Clin 50 (1), 65-76 (2009)Yilmaz,M., Yurtcu,E. J. Endocrinol. Invest. 32 (1), 13-17 (2009)Evans,J.C., Frayling,T.M. Am. J. Hum. Genet. 69 (3), 544-552 (2001)
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